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PDB id:
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Transferase
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Title:
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Crystal structure of RNA polymerase pb1-pb2 subunits from influenza a virus
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Structure:
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RNA-directed RNA polymerase catalytic subunit. Chain: a, c. Fragment: pb1 c-terminal fragment, unp residues 679-757. Synonym: RNA polymerase pb1 subunit, polymerase basic protein 1, pb1, RNA-directed RNA polymerase subunit p1. Engineered: yes. Polymerase basic protein 2. Chain: b, d. Fragment: pb2 n-terminal ragment, unp residues 1-37.
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Source:
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Influenza a virus (a/puerto rico/8/34(h1n1)). Organism_taxid: 211044. Gene: pb1. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: pb2.
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Resolution:
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2.10Å
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R-factor:
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0.235
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R-free:
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0.272
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Authors:
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K.Sugiyama,E.Obayashi,S.-Y.Park
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Key ref:
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K.Sugiyama
et al.
(2009).
Structural insight into the essential PB1-PB2 subunit contact of the influenza virus RNA polymerase.
Embo J,
28,
1803-1811.
PubMed id:
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Date:
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08-Oct-08
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Release date:
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09-Jun-09
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PROCHECK
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Headers
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References
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Enzyme class:
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Chains A, C:
E.C.2.7.7.48
- RNA-directed Rna polymerase.
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Reaction:
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RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
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RNA(n)
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+
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ribonucleoside 5'-triphosphate
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=
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RNA(n+1)
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+
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diphosphate
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Embo J
28:1803-1811
(2009)
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PubMed id:
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Structural insight into the essential PB1-PB2 subunit contact of the influenza virus RNA polymerase.
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K.Sugiyama,
E.Obayashi,
A.Kawaguchi,
Y.Suzuki,
J.R.Tame,
K.Nagata,
S.Y.Park.
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ABSTRACT
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Influenza virus RNA-dependent RNA polymerase is a multi-functional heterotrimer,
which uses a 'cap-snatching' mechanism to produce viral mRNA. Host cell mRNA is
cleaved to yield a cap-bearing oligonucleotide, which can be extended using
viral genomic RNA as a template. The cap-binding and endonuclease activities are
only activated once viral genomic RNA is bound. This requires signalling from
the RNA-binding PB1 subunit to the cap-binding PB2 subunit, and the interface
between these two subunits is essential for the polymerase activity. We have
defined this interaction surface by protein crystallography and tested the
effects of mutating contact residues on the function of the holo-enzyme. This
novel interface is surprisingly small, yet, it has a crucial function in
regulating the 250 kDa polymerase complex and is completely conserved among
avian and human influenza viruses.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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Y.An,
P.Meresse,
P.J.Mas,
and
D.J.Hart
(2011).
CoESPRIT: A Library-Based Construct Screening Method for Identification and Expression of Soluble Protein Complexes.
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PLoS One,
6,
e16261.
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B.G.Hale,
R.A.Albrecht,
and
A.García-Sastre
(2010).
Innate immune evasion strategies of influenza viruses.
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Future Microbiol,
5,
23-41.
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J.T.Perez,
A.Varble,
R.Sachidanandam,
I.Zlatev,
M.Manoharan,
A.García-Sastre,
and
B.R.tenOever
(2010).
Influenza A virus-generated small RNAs regulate the switch from transcription to replication.
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Proc Natl Acad Sci U S A,
107,
11525-11530.
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K.Das,
J.M.Aramini,
L.C.Ma,
R.M.Krug,
and
E.Arnold
(2010).
Structures of influenza A proteins and insights into antiviral drug targets.
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Nat Struct Mol Biol,
17,
530-538.
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K.M.Graef,
F.T.Vreede,
Y.F.Lau,
A.W.McCall,
S.M.Carr,
K.Subbarao,
and
E.Fodor
(2010).
The PB2 subunit of the influenza virus RNA polymerase affects virulence by interacting with the mitochondrial antiviral signaling protein and inhibiting expression of beta interferon.
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J Virol,
84,
8433-8445.
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M.A.Mir,
S.Sheema,
A.Haseeb,
and
A.Haque
(2010).
Hantavirus nucleocapsid protein has distinct m7G cap- and RNA-binding sites.
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J Biol Chem,
285,
11357-11368.
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P.Resa-Infante,
M.A.Recuero-Checa,
N.Zamarreño,
O.Llorca,
and
J.Ortín
(2010).
Structural and functional characterization of an influenza virus RNA polymerase-genomic RNA complex.
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J Virol,
84,
10477-10487.
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S.Huet,
S.V.Avilov,
L.Ferbitz,
N.Daigle,
S.Cusack,
and
J.Ellenberg
(2010).
Nuclear import and assembly of influenza A virus RNA polymerase studied in live cells by fluorescence cross-correlation spectroscopy.
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J Virol,
84,
1254-1264.
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S.R.Shih,
J.T.Horng,
L.L.Poon,
T.C.Chen,
J.Y.Yeh,
H.P.Hsieh,
S.N.Tseng,
C.Chiang,
W.L.Li,
Y.S.Chao,
and
J.T.Hsu
(2010).
BPR2-D2 targeting viral ribonucleoprotein complex-associated function inhibits oseltamivir-resistant influenza viruses.
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J Antimicrob Chemother,
65,
63-71.
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T.Fislová,
B.Thomas,
K.M.Graef,
and
E.Fodor
(2010).
Association of the influenza virus RNA polymerase subunit PB2 with the host chaperonin CCT.
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J Virol,
84,
8691-8699.
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E.Nistal-Villán,
and
A.García-Sastre
(2009).
New prospects for the rational design of antivirals.
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Nat Med,
15,
1253-1254.
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K.Wunderlich,
D.Mayer,
C.Ranadheera,
A.S.Holler,
B.Mänz,
A.Martin,
G.Chase,
W.Tegge,
R.Frank,
U.Kessler,
and
M.Schwemmle
(2009).
Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication.
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PLoS One,
4,
e7517.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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